Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Bioenergetics

Two phases of proton translocation

Nature volume 400, pages 412–413 (1999)Cite this article

The ‘central dogma’ of bioenergetics is the chemiosmotic theory, which states that energy stored as a proton gradient across biological membranes (the proton-motive force) is converted to useful chemical energy in the form of ATP. In eukaryotes, the proton-motive force is generated across the inner membrane of the mitochondria by harnessing the energy released from serial electron-transfer events in membrane-bound proteins. This chain culminates in the four-electron reduction of oxygen to water by an enzyme called cytochrome c oxidase. Associated with this oxygen chemistry, four protons are pumped across the membrane in opposition to a proton gradient1.

The molecular mechanism by which oxygen reduction is coupled to proton translocation — the redox linkage — remains a central question. Guided by spectroscopic2,3, crystallographic4,5 and mutagenesis6 results, several models for redox linkage have been proposed, but each has its flaws. One feature that has been lacking is a quantitative temporal relationship between the chemical steps and the translocation of protons7. On page 480 of this issue, Mårten Wikström and co-workers8 propose a surprising time frame for this relationship.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Proton pumping in cytochrome c oxidase, based on the results of Wikström and colleagues8

References

  1. Babcock, G. T. & Wikström, M. Nature 356, 301–309 (1992).

    Google Scholar 

  2. Han, S., Ching, Y.-c. & Rousseau, D. L. Nature 348, 89–90 (1990).

    Google Scholar 

  3. Ferguson-Miller, S. & Babcock, G. T. Chem. Rev. 96, 2889–2907 (1996).

    Google Scholar 

  4. Tsukihara, T. et al. Science 269, 1069–1074 (1995).

    Google Scholar 

  5. Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. Nature 376, 660–669 (1995).

    Google Scholar 

  6. Gennis, R. B. Biochim. Biophys. Acta 1365, 241–248 (1998).

    Google Scholar 

  7. Gennis, R. B. Proc. Natl Acad. Sci. USA 95, 12747–12749 (1998).

    Google Scholar 

  8. Verhovsky, M. I., Jasaitis, A., Verhovskaya, M. L., Morgan, J. E. & Wikström, M. Nature 400, 480–483 (1999).

    Google Scholar 

  9. Wikström, M. Nature 338, 776–778 (1989).

    Google Scholar 

  10. Michel, H. Proc. Natl Acad. Sci. USA 95, 12819–12824 (1998).

    Google Scholar 

  11. Mitchell, R., Mitchell, P. & Rich, P. R. Biochim. Biophys. Acta 1101, 188–191 (1992).

    Google Scholar 

  12. Osborne, J. P. et al. Biochemistry 38, 4526–4532 (1999).

    Google Scholar 

  13. Friedman, J. M. Science 228, 1273–1280 (1985).

    Google Scholar 

  14. Sassaroli, M., Ching, Y.-c., Argade, P. V. & Rousseau, D. L. Biochemistry 27, 2496–2502 (1988).

    Google Scholar 

  15. Findsen, E. W., Centeno, J., Babcock, G. T. & Ondrias, M. R. J. Am. Chem. Soc. 109, 5367–5372 (1987).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, 10461, New York, USA

    Denis L. Rousseau

Authors
  1. Denis L. Rousseau
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Rousseau, D. Two phases of proton translocation. Nature 400, 412–413 (1999). https://doi.org/10.1038/22664

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/22664

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing